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1TAS

CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006103biological_process2-oxoglutarate metabolic process
A0006520biological_processamino acid metabolic process
A0006531biological_processaspartate metabolic process
A0006533biological_processaspartate catabolic process
A0006536biological_processglutamate metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006103biological_process2-oxoglutarate metabolic process
B0006520biological_processamino acid metabolic process
B0006531biological_processaspartate metabolic process
B0006533biological_processaspartate catabolic process
B0006536biological_processglutamate metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLA A 411
ChainResidue
AILE17
AVAL37
AGLY38
ASER107
AGLY108
ATHR109
ATRP140
AASN194
AASP222
AALA224
ATYR225
ASER255
ALYS258
AARG266
AARG386
BTYR70
BARG292

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLA B 411
ChainResidue
ATYR70
AARG292
BILE17
BVAL37
BGLY38
BSER107
BGLY108
BTHR109
BTRP140
BASN194
BASP222
BTYR225
BSER255
BLYS258
BARG266
BARG386

site_idACT
Number of Residues24
DetailsACTIVE SITE, COMPRISE THE RESIDUES INTERACTING WITH THE COENZYME-INHIBITOR ADDUCT
ChainResidue
AASP15
ATHR109
ATRP140
AASN194
AASP222
AALA224
ATYR225
ASER255
ALYS258
AARG266
BARG292
AILE17
BSER296
BASN297
APHE360
AARG386
APLA411
ALEU18
AVAL37
AGLY38
AALA39
BTYR70
ASER107
AGLY108

site_idBCT
Number of Residues24
DetailsACTIVE SITE, COMPRISE THE RESIDUES INTERACTING WITH THE COENZYME-INHIBITOR ADDUCT
ChainResidue
BASP15
BILE17
BLEU18
BVAL37
BGLY38
BALA39
ATYR70
BSER107
BGLY108
BTHR109
BTRP140
BASN194
BASP222
BALA224
BTYR225
BSER255
BLYS258
BARG266
AARG292
ASER296
AASN297
BPHE360
BARG386
BPLA411

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERAG
ChainResidueDetails
ASER255-GLY268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLY38
ATRP140
AASN194
AARG386
BGLY38
BTRP140
BASN194
BARG386

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS258
BLYS258

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222
ALYS258

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP140
BASP222
BLYS258

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP140
BASP222

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PDB entries from 2024-10-30

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